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A1SYV1 (LPXA_PSYIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase

Short name=UDP-N-acetylglucosamine acyltransferase
EC=2.3.1.129
Gene names
Name:lpxA
Ordered Locus Names:Ping_2964
OrganismPsychromonas ingrahamii (strain 37) [Complete proteome] [HAMAP]
Taxonomic identifier357804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPsychromonadaceaePsychromonas

Protein attributes

Sequence length262 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell By similarity. HAMAP-Rule MF_00387

Catalytic activity

(R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] + UDP-N-acetyl-alpha-D-glucosamine = [acyl-carrier-protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine. HAMAP-Rule MF_00387

Pathway

Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. HAMAP-Rule MF_00387

Subunit structure

Homotrimer By similarity. HAMAP-Rule MF_00387

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00387.

Sequence similarities

Belongs to the transferase hexapeptide repeat family. LpxA subfamily.

Ontologies

Keywords
   Biological processLipid A biosynthesis
Lipid biosynthesis
Lipid metabolism
   Cellular componentCytoplasm
   DomainRepeat
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processlipid A biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 262262Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase HAMAP-Rule MF_00387
PRO_0000302594

Sequences

Sequence LengthMass (Da)Tools
A1SYV1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 6D8FF84D001AB2B5

FASTA26228,641
        10         20         30         40         50         60 
MTKKIAMIHP TAIVHENAII GKDVEIGPYT IIGDRVEIGD NCWIAPHVVI KGPTKMGKGN 

        70         80         90        100        110        120 
KIYQFASIGE DCQDLKYNGE ETFLEIGDNN VFRESCTVHR GTAQDQGTTR IGNNNLLMAY 

       130        140        150        160        170        180 
VHVAHDCVLG NNIILSNNAT LAGHTKLANN VIIGGLSALH QFTRVGEFAM IGGCSAVNKD 

       190        200        210        220        230        240 
IPPYFMATGN YVEAQGVNSV GLKRSGFNSK AIMEIKRAYK ILCREGNSLE QAKIKIAEKL 

       250        260 
EGCPELQVLY DFICEESRGI VR 

« Hide

References

[1]"Complete sequence of Psychromonas ingrahamii 37."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Ivanova N., Staley J., Richardson P.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 37.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000510 Genomic DNA. Translation: ABM04666.1.
RefSeqYP_944265.1. NC_008709.1.

3D structure databases

ProteinModelPortalA1SYV1.
SMRA1SYV1. Positions 1-262.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING357804.Ping_2964.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM04666; ABM04666; Ping_2964.
GeneID4623480.
KEGGpin:Ping_2964.
PATRIC23071381. VBIPsyIng103130_3273.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1043.
HOGENOMHOG000294326.
KOK00677.
OMADCQDKKY.
OrthoDBEOG6F81P1.

Enzyme and pathway databases

BioCycPING357804:GJBJ-3069-MONOMER.
UniPathwayUPA00359; UER00477.

Family and domain databases

Gene3D1.20.1180.10. 1 hit.
HAMAPMF_00387. LpxA.
InterProIPR029098. Acetyltransf_C.
IPR001451. Hexapep_transf.
IPR010137. Lipid_A_LpxA.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF13720. Acetyltransf_11. 1 hit.
PF00132. Hexapep. 3 hits.
[Graphical view]
PIRSFPIRSF000456. UDP-GlcNAc_acltr. 1 hit.
SUPFAMSSF51161. SSF51161. 1 hit.
TIGRFAMsTIGR01852. lipid_A_lpxA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLPXA_PSYIN
AccessionPrimary (citable) accession number: A1SYV1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 6, 2007
Last modified: June 11, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways